4onq: Difference between revisions
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==Crystal structure of ntDRM E283S/R309S/F310S/Y590S/D591S mutant== | ==Crystal structure of ntDRM E283S/R309S/F310S/Y590S/D591S mutant== | ||
<StructureSection load='4onq' size='340' side='right' caption='[[4onq]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4onq' size='340' side='right' caption='[[4onq]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4onj|4onj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4onj|4onj]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4onq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4onq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4onq RCSB], [http://www.ebi.ac.uk/pdbsum/4onq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4onq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4onq OCA], [http://pdbe.org/4onq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4onq RCSB], [http://www.ebi.ac.uk/pdbsum/4onq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4onq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4onq" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:11, 11 August 2016
Crystal structure of ntDRM E283S/R309S/F310S/Y590S/D591S mutantCrystal structure of ntDRM E283S/R309S/F310S/Y590S/D591S mutant
Structural highlights
Publication Abstract from PubMedDNA methylation is a conserved epigenetic gene-regulation mechanism. DOMAINS REARRANGED METHYLTRANSFERASE (DRM) is a key de novo methyltransferase in plants, but how DRM acts mechanistically is poorly understood. Here, we report the crystal structure of the methyltransferase domain of tobacco DRM (NtDRM) and reveal a molecular basis for its rearranged structure. NtDRM forms a functional homodimer critical for catalytic activity. We also show that Arabidopsis DRM2 exists in complex with the small interfering RNA (siRNA) effector ARGONAUTE4 (AGO4) and preferentially methylates one DNA strand, likely the strand acting as the template for RNA polymerase V-mediated noncoding RNA transcripts. This strand-biased DNA methylation is also positively correlated with strand-biased siRNA accumulation. These data suggest a model in which DRM2 is guided to target loci by AGO4-siRNA and involves base-pairing of associated siRNAs with nascent RNA transcripts. Molecular Mechanism of Action of Plant DRM De Novo DNA Methyltransferases.,Zhong X, Du J, Hale CJ, Gallego-Bartolome J, Feng S, Vashisht AA, Chory J, Wohlschlegel JA, Patel DJ, Jacobsen SE Cell. 2014 May 22;157(5):1050-60. doi: 10.1016/j.cell.2014.03.056. PMID:24855943[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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